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Protein

Molybdopterin molybdenumtransferase

Gene

moeA

Organism
Escherichia coli (strain K12)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Catalyzes the insertion of molybdate into adenylated molybdopterin with the concomitant release of AMP.1 Publication

Catalytic activityi

Adenylyl-molybdopterin + molybdate = molybdenum cofactor + AMP.

Cofactori

Mg2+1 PublicationNote: Binds 1 Mg2+ ion per subunit.1 Publication

Pathwayi: molybdopterin biosynthesis

This protein is involved in the pathway molybdopterin biosynthesis, which is part of Cofactor biosynthesis.
View all proteins of this organism that are known to be involved in the pathway molybdopterin biosynthesis and in Cofactor biosynthesis.

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Transferase

Keywords - Biological processi

Molybdenum cofactor biosynthesis

Keywords - Ligandi

Magnesium, Metal-binding, Molybdenum

Enzyme and pathway databases

BioCyciEcoCyc:EG10153-MONOMER.
ECOL316407:JW0811-MONOMER.
MetaCyc:EG10153-MONOMER.
BRENDAi2.10.1.1. 2026.
UniPathwayiUPA00344.

Names & Taxonomyi

Protein namesi
Recommended name:
Molybdopterin molybdenumtransferase (EC:2.10.1.1)
Short name:
MPT Mo-transferase
Gene namesi
Name:moeA
Synonyms:bisB, chlE, narE
Ordered Locus Names:b0827, JW0811
OrganismiEscherichia coli (strain K12)
Taxonomic identifieri83333 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacteralesEnterobacteriaceaeEscherichia
Proteomesi
  • UP000000318 Componenti: Chromosome
  • UP000000625 Componenti: Chromosome

Organism-specific databases

EcoGeneiEG10153. moeA.

Subcellular locationi

GO - Cellular componenti

  • cytosol Source: EcoCyc
Complete GO annotation...

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001709891 – 411Molybdopterin molybdenumtransferaseAdd BLAST411

Proteomic databases

EPDiP12281.
PaxDbiP12281.
PRIDEiP12281.

Interactioni

Subunit structurei

Homodimer. Interacts with MobA, MogA and MobB in vivo.3 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
mobAP321733EBI-554393,EBI-1133881

Protein-protein interaction databases

BioGridi4259979. 8 interactors.
DIPiDIP-10240N.
IntActiP12281. 8 interactors.
MINTiMINT-1250871.
STRINGi511145.b0827.

Structurei

Secondary structure

1411
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi10 – 20Combined sources11
Beta strandi27 – 31Combined sources5
Helixi32 – 34Combined sources3
Beta strandi39 – 42Combined sources4
Beta strandi50 – 53Combined sources4
Beta strandi55 – 63Combined sources9
Helixi65 – 70Combined sources6
Beta strandi76 – 81Combined sources6
Beta strandi82 – 84Combined sources3
Beta strandi95 – 98Combined sources4
Beta strandi110 – 113Combined sources4
Helixi114 – 116Combined sources3
Beta strandi117 – 120Combined sources4
Beta strandi123 – 126Combined sources4
Turni132 – 135Combined sources4
Beta strandi141 – 143Combined sources3
Beta strandi147 – 150Combined sources4
Turni158 – 160Combined sources3
Helixi161 – 166Combined sources6
Beta strandi171 – 175Combined sources5
Beta strandi179 – 185Combined sources7
Beta strandi187 – 190Combined sources4
Beta strandi192 – 194Combined sources3
Helixi205 – 215Combined sources11
Beta strandi219 – 226Combined sources8
Helixi230 – 243Combined sources14
Beta strandi245 – 249Combined sources5
Beta strandi251 – 253Combined sources3
Beta strandi255 – 257Combined sources3
Helixi260 – 268Combined sources9
Beta strandi269 – 280Combined sources12
Beta strandi283 – 288Combined sources6
Beta strandi290 – 296Combined sources7
Helixi301 – 310Combined sources10
Helixi312 – 320Combined sources9
Beta strandi326 – 328Combined sources3
Beta strandi331 – 337Combined sources7
Beta strandi345 – 355Combined sources11
Beta strandi357 – 359Combined sources3
Beta strandi361 – 365Combined sources5
Helixi376 – 379Combined sources4
Beta strandi381 – 386Combined sources6
Beta strandi398 – 403Combined sources6
Helixi406 – 408Combined sources3

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1FC5X-ray2.20A/B1-411[»]
1G8LX-ray1.95A/B1-411[»]
1G8RX-ray2.65A/B1-411[»]
2NQKX-ray2.90A/B1-411[»]
2NQMX-ray3.00A/B1-411[»]
2NQNX-ray2.20A/B1-411[»]
2NQQX-ray2.40A/B/C/D1-411[»]
2NQRX-ray2.20A/B1-411[»]
2NQSX-ray2.50A/B1-411[»]
2NQUX-ray2.70A/B1-411[»]
2NQVX-ray2.82A/B1-411[»]
2NROX-ray2.50A/B1-411[»]
2NRPX-ray3.00A/B1-411[»]
2NRSX-ray2.80A/B1-411[»]
ProteinModelPortaliP12281.
SMRiP12281.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP12281.

Family & Domainsi

Sequence similaritiesi

Belongs to the MoeA family.Curated

Phylogenomic databases

eggNOGiENOG4105CVM. Bacteria.
COG0303. LUCA.
HOGENOMiHOG000280652.
InParanoidiP12281.
KOiK03750.
OMAiFALAPKD.
PhylomeDBiP12281.

Family and domain databases

Gene3Di2.40.340.10. 1 hit.
3.40.980.10. 1 hit.
InterProiIPR001453. MoaB/Mog_dom.
IPR008284. MoCF_biosynth_CS.
IPR005111. MoeA_C_domain_IV.
IPR005110. MoeA_linker/N.
[Graphical view]
PfamiPF00994. MoCF_biosynth. 1 hit.
PF03454. MoeA_C. 1 hit.
PF03453. MoeA_N. 1 hit.
[Graphical view]
SMARTiSM00852. MoCF_biosynth. 1 hit.
[Graphical view]
SUPFAMiSSF53218. SSF53218. 1 hit.
SSF63867. SSF63867. 1 hit.
SSF63882. SSF63882. 1 hit.
TIGRFAMsiTIGR00177. molyb_syn. 1 hit.
PROSITEiPS01079. MOCF_BIOSYNTHESIS_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P12281-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MEFTTGLMSL DTALNEMLSR VTPLTAQETL PLVQCFGRIL ASDVVSPLDV
60 70 80 90 100
PGFDNSAMDG YAVRLADIAS GQPLPVAGKS FAGQPYHGEW PAGTCIRIMT
110 120 130 140 150
GAPVPEGCEA VVMQEQTEQM DNGVRFTAEV RSGQNIRRRG EDISAGAVVF
160 170 180 190 200
PAGTRLTTAE LPVIASLGIA EVPVIRKVRV ALFSTGDELQ LPGQPLGDGQ
210 220 230 240 250
IYDTNRLAVH LMLEQLGCEV INLGIIRDDP HALRAAFIEA DSQADVVISS
260 270 280 290 300
GGVSVGEADY TKTILEELGE IAFWKLAIKP GKPFAFGKLS NSWFCGLPGN
310 320 330 340 350
PVSATLTFYQ LVQPLLAKLS GNTASGLPAR QRVRTASRLK KTPGRLDFQR
360 370 380 390 400
GVLQRNADGE LEVTTTGHQG SHIFSSFSLG NCFIVLERDR GNVEVGEWVE
410
VEPFNALFGG L
Length:411
Mass (Da):44,067
Last modified:October 1, 1989 - v1
Checksum:i6DBBC2B4191F5951
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M21151 Genomic DNA. Translation: AAA23579.1.
U00096 Genomic DNA. Translation: AAC73914.1.
AP009048 Genomic DNA. Translation: BAA35515.1.
PIRiA32352.
RefSeqiNP_415348.1. NC_000913.3.
WP_000397340.1. NZ_LN832404.1.

Genome annotation databases

EnsemblBacteriaiAAC73914; AAC73914; b0827.
BAA35515; BAA35515; BAA35515.
GeneIDi945454.
KEGGiecj:JW0811.
eco:b0827.
PATRICi32116857. VBIEscCol129921_0854.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M21151 Genomic DNA. Translation: AAA23579.1.
U00096 Genomic DNA. Translation: AAC73914.1.
AP009048 Genomic DNA. Translation: BAA35515.1.
PIRiA32352.
RefSeqiNP_415348.1. NC_000913.3.
WP_000397340.1. NZ_LN832404.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1FC5X-ray2.20A/B1-411[»]
1G8LX-ray1.95A/B1-411[»]
1G8RX-ray2.65A/B1-411[»]
2NQKX-ray2.90A/B1-411[»]
2NQMX-ray3.00A/B1-411[»]
2NQNX-ray2.20A/B1-411[»]
2NQQX-ray2.40A/B/C/D1-411[»]
2NQRX-ray2.20A/B1-411[»]
2NQSX-ray2.50A/B1-411[»]
2NQUX-ray2.70A/B1-411[»]
2NQVX-ray2.82A/B1-411[»]
2NROX-ray2.50A/B1-411[»]
2NRPX-ray3.00A/B1-411[»]
2NRSX-ray2.80A/B1-411[»]
ProteinModelPortaliP12281.
SMRiP12281.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi4259979. 8 interactors.
DIPiDIP-10240N.
IntActiP12281. 8 interactors.
MINTiMINT-1250871.
STRINGi511145.b0827.

Proteomic databases

EPDiP12281.
PaxDbiP12281.
PRIDEiP12281.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAC73914; AAC73914; b0827.
BAA35515; BAA35515; BAA35515.
GeneIDi945454.
KEGGiecj:JW0811.
eco:b0827.
PATRICi32116857. VBIEscCol129921_0854.

Organism-specific databases

EchoBASEiEB0151.
EcoGeneiEG10153. moeA.

Phylogenomic databases

eggNOGiENOG4105CVM. Bacteria.
COG0303. LUCA.
HOGENOMiHOG000280652.
InParanoidiP12281.
KOiK03750.
OMAiFALAPKD.
PhylomeDBiP12281.

Enzyme and pathway databases

UniPathwayiUPA00344.
BioCyciEcoCyc:EG10153-MONOMER.
ECOL316407:JW0811-MONOMER.
MetaCyc:EG10153-MONOMER.
BRENDAi2.10.1.1. 2026.

Miscellaneous databases

EvolutionaryTraceiP12281.
PROiP12281.

Family and domain databases

Gene3Di2.40.340.10. 1 hit.
3.40.980.10. 1 hit.
InterProiIPR001453. MoaB/Mog_dom.
IPR008284. MoCF_biosynth_CS.
IPR005111. MoeA_C_domain_IV.
IPR005110. MoeA_linker/N.
[Graphical view]
PfamiPF00994. MoCF_biosynth. 1 hit.
PF03454. MoeA_C. 1 hit.
PF03453. MoeA_N. 1 hit.
[Graphical view]
SMARTiSM00852. MoCF_biosynth. 1 hit.
[Graphical view]
SUPFAMiSSF53218. SSF53218. 1 hit.
SSF63867. SSF63867. 1 hit.
SSF63882. SSF63882. 1 hit.
TIGRFAMsiTIGR00177. molyb_syn. 1 hit.
PROSITEiPS01079. MOCF_BIOSYNTHESIS_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiMOEA_ECOLI
AccessioniPrimary (citable) accession number: P12281
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1989
Last sequence update: October 1, 1989
Last modified: November 2, 2016
This is version 153 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Escherichia coli
    Escherichia coli (strain K12): entries and cross-references to EcoGene
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.